An annotated selection of World Wide Web sites relevant to the topics ... respective microbial host. Peptidase ... lividans to be a particularly good secretion host.
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Web alert Microbial enzyme secretion An annotated selection of World Wide Web sites relevant to the topics in microbial biotechnology. Fungal secretome knowledge base
The Fungal Secretome KnowledgeBase contains data from many fungi. One can look for secreted proteins or input a particular protein to see whether it is secreted.
This review is on bacterial secretion systems with a major focus on their role in promoting bacterial virulence.
Database of lignocellulose-degrading enzymes from fungi
Type three secretion system https://en.wikipedia.org/wiki/Type_three_secretion_system
https://mycoclap.fungalgenomics.ca/mycoCLAP/
This Wikipedia entry provides a fairly comprehensive overview of bacterial type III secretion systems.
This database focuses on fungal, and some bacterial, enzymes that have activity against lignocellulose materials. Many of those enzymes are secreted from their respective microbial host.
X-ray structure of a type III secretion system component https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4400350/
Peptidase database http://merops.sanger.ac.uk/cgi-bin/name_index?id=P; action=A This database focuses on protease and peptidase enzymes. Many microbes living in soil environments secrete proteases to break down proteins into amino acids and peptides that can be transported into the cell. Database for type IV secretion system http://www.t4ss.lncc.br This small database is focused on bacterial type IV secretion systems. Identification of secretion systems in bacterial genomes
This paper deals with the structure of a protein component that aids the process by which type III secretion systems traverse the peptidoglycan layer. Killing via a type IV secretion system http://www.nature.com/articles/ncomms7453 This study shows that the type IV secretion system of Xanthomonas citri can kill other Gram-negative bacteria in a contact-dependent manner. OmpA-facilitated chitinase secretion https://springerplus.springeropen.com/articles/10.1186/ s40064-016-2893-y
http://www.nature.com/articles/srep23080
Protein modification with a OmpA signal peptide was most productive with respect to secretion of a Bacillus chitinase by E. coli.
This relatively recent publication deals with computational methods for identifying secretion system genes in genomic sequences.
Streptomyces protein secretion biotechnology http://www.sciencedirect.com/science/article/pii/ S0167488914000093
ª 2017 The Authors. Microbial Biotechnology published by John Wiley & Sons Ltd and Society for Applied Microbiology. This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
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Web alert
Many Bacillus and Streptomyces strains are good protein secretors. This study demonstrated Streptomyces lividans to be a particularly good secretion host.
The review details the use of Pichia for producing carbohydrate-hydrolysing enzymes that are highly useful in biodegrading biomass.
Optimization of protein secretion by Bacillus subtilis
Patent on protease deficient Pichia secretion strain
https://www.ncbi.nlm.nih.gov/pubmed/19075856
https://www.google.com/patents/US8703444
This article deals mostly with commercially important aspects of Bacillus secretion systems and reviews recent patents in the area.
Naturally produced proteins can cause problems in highlevel expression of heterologous proteins, and this patent describes a protease deficient mutant that aids expression of intact protein.
Phytase secretion by Bacillus subtilis http://www.tandfonline.com/doi/pdf/10.1080/09168451. 2015.1046366
Phytases are industrially important enzymes for their ability to release phosphate from phytic acid. This study explores its secretion by a Bacillus strain.
This commercial website contains much useful information on the construction and use of Pichia expression and secretion systems.
Secretion of a thermostable amylase
High-level protein production in Streptomyces lividans
http://www.nature.com/articles/srep22229 An amylase from Pyrococcus furiosus is significant industrially because of its stability at high temperatures and low pH. It is shown here to be secreted by a Bacillus amyloliquefaciens strain.
https://microbialcellfactories.biomedcentral.com/articles/ 10.1186/s12934-016-0425-7 An amylase, laccase and xylanase were used as reporters to optimize secreted expression in Streptomyces lividans.
Protein secretion by Pichia pastoris review https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4047484/
Development of a Corynebacterium glutamicum secretion system
Pichia is a methylotrophic yeast that grows to high cell density, and this review offers ideas for optimizing protein secretion by this strain.
Methyl parathion hydrolase secretion by Pichia http://journals.plos.org/plosone/article?id=10.1371/journal. pone.0096974 This paper deals with the secretion of an enzyme for biodegrading a common pesticide. Pichia technology http://www.pichia.com This commercial site contains significant and useful information on Pichia and its secretion systems.
Corynebacterium glutamicum is a very important industrial strain for amino acid production. This study investigated establishing this microbe for protein secretion. Aspergillus protein secretion http://bmcsystbiol.biomedcentral.com/articles/10.1186/ 1752-0509-8-73 Aspergillus oryzae is an important strain for secreting industrial enzymes, and it also performs necessary posttranslational modifications. This study was conducted to better understand the fundamental molecular machinery involved.
Pichia secretion tools https://www.thermofisher.com/order/catalog/product/A11155 This commercial page has lnks to information on Pichia. Fungal biomass degrading enzymes from Pichia
Lawrence P. Wackett McKnight Professor Department of Biochemistry, Molecular Biology and Biophysics, BioTechnology Institute, University of Minnesota, St Paul, MN 55108, USA
http://journal.frontiersin.org/article/10.3389/fmicb.2015. 01002/full ª 2017 The Authors. Microbial Biotechnology published by John Wiley & Sons Ltd and Society for Applied Microbiology, Microbial Biotechnology, 10, 513–514
